Chloroplast and Cytosol Isozymes of Cu, Zn-Superoxide Dismutase: Their Characteristic Amino Acid Sequences

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Abstract
Isozymes of CuZn-superoxide dismutase (SOD) were purified from angiosperms (spinach and rice), fern (horsetail) and green alga (Spirogyra). Occurrence of CuZn-SOD was confirmed by its purification in the group of green algae which shows the phragmoplast type of cell division. Purified CuZn-SODs are divided to chloroplast and cytosol types by their cellular localization and immunological properties. Their amino acid compositions, absorption spectra, CD spectra, and sensitivity to hydrogen peroxide also are distinguished from each other. All organisms including Spirogyra contain both types of isozyme. Thus, the divergence of the two types of CuZn-SOD isozyme occurred immediately after its acquisition by the most evolved green algae. Amino acid sequences of amino-terminal regions of CuZn-SOD isozymes from spinach, rice and horsetail were determined and compared with those of CuZn-SODs from other plants. The chloroplast and cytosol isozymes of CuZn-SOD show each characteristic sequences. Sequence differences among the cytosol CuZn-SODs are greater than those among the chloroplast CuZn-SODs. These observations indicate that each type of isozyme had independently evolved after the acquisition of CuZn-SOD.

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